Evidence map›Paper›PMID 29880877›Full record

ArticleOncogene2018

Stratifin regulates stabilization of receptor tyrosine kinases via interaction with ubiquitin-specific protease 8 in lung adenocarcinoma.

Yunjung Kim, Aya Shiba-Ishii, Tomoki Nakagawa, Shun-Ichiro Iemura, Tohru Natsume, Noriyuki Nakano, Ryota Matsuoka, Shingo Sakashita, SangJoon Lee, Atsushi Kawaguchi and 2 more

Abstract read
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In one paragraph

Article in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 44 citations in OpenAlex.

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  15. Quantitative Expression ofGenetics research · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Yunjung KimDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Aya Shiba-IshiiDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan. aya_shiba@md.tsukuba.ac.jp.ORCID http://orcid.org/0000-0001-6639-4135
Tomoki NakagawaDoctoral Program in Biomedical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba, Ibaraki, Japan.
Shun-Ichiro IemuraTranslational Research Center, Fukushima Medical University, Fukushima, Japan.
Tohru NatsumeMolecular Profiling Research Center for Drug Discovery, National Institutes of Advanced Industrial Science and Technology, Tokyo, Japan.
Noriyuki NakanoDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Ryota MatsuokaDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Shingo SakashitaDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
SangJoon LeePh.D. Program in Human Biology, School of Integrative and Global Majors, University of Tsukuba, Ibaraki, Japan.
Atsushi KawaguchiDepartment of Infection Biology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Yukio SatoDepartment of Thoracic Surgery, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan.
Masayuki NoguchiDepartment of Pathology, Faculty of Medicine, University of Tsukuba, Ibaraki, Japan. nmasayuk@md.tsukuba.ac.jp.
University of Tsukuba · JPFukushima Medical University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previously we have reported that stratifin (SFN, 14-3-3 sigma) acts as a novel oncogene, accelerating the tumor initiation and progression of lung adenocarcinoma. Here, pull-down assay and LC-MS/MS analysis revealed that ubiquitin-specific protease 8 (USP8) specifically bound to SFN in lung adenocarcinoma cells. Both USP8 and SFN showed higher expression in human lung adenocarcinoma than in normal lung tissue, and USP8 expression was significantly correlated with SFN expression. Expression of SFN, but not of USP8, was associated with histological subtype, pathological stage, and poor prognosis. USP8 stabilizes receptor tyrosine kinases (RTKs) such as EGFR and MET by deubiquitination, contributing to the proliferative activity of many human cancers including non-small cell lung cancer. In vitro, USP8 binds to SFN and they co-localize at the early endosomes in lung adenocarcinoma cells. Moreover, USP8 or SFN knockdown leads to downregulation of tumor cellular proliferation and upregulation of apoptosis, p-EGFR or p-MET, which are related to the degradation pathway, and accumulation of ubiquitinated RTKs, leading to lysosomal degradation. Additionally, mutant USP8, which is unable to bind to SFN, reduces the expression of RTKs and p-STAT3. We also found that interaction with SFN is critical for USP8 to exert its autodeubiquitination function and avoid dephosphorylation by PP1. Our findings demonstrate that SFN enhances RTK stabilization through abnormal USP8 regulation in lung adenocarcinoma, suggesting that SFN could be a more suitable therapeutic target for lung adenocarcinoma than USP8.

Indexed as

14-3-3 ProteinsAdenocarcinoma of LungApoptosisBiomarkers, TumorCell Line, TumorCell ProliferationEndopeptidasesEndosomal Sorting Complexes Required for TransportExoribonucleasesGene Expression Regulation, NeoplasticHumansProtein BindingProteolysisReceptor Protein-Tyrosine KinasesUbiquitin Thiolesterase14-3-3 ProteinsBiomarkers, TumorEndopeptidasesEndosomal Sorting Complexes Required for TransportExoribonucleasesReceptor Protein-Tyrosine KinasesSFN protein, humanUbiquitin ThiolesteraseUSP8 protein, human

Identifiers

PMID29880877
OpenAlexW2805313167

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.